Metacaspase activity of Arabidopsis thaliana is regulated by S-nitrosylation of a critical cysteine residue

Journal of Biological Chemistry

Volumn 282, Issue 2, 2007, Pages 1352-1358

  Belenghi, Beatrice ^a   Romero Puertas, Maria C ^a,c   Vercammen, Dominique ^a   Brackenier, Anouk ^a   Inzé, Dirk ^a   Delledonne, Massimo ^b   Van Breusegem, Frank ^a  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^b UNIVERSITY OF VERONA   (Italy)

^c JOHN INNES CENTRE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPROCESSING; CYSTEINE; NITROSOTHIOL;

AMINO ACIDS; ENZYME ACTIVITY; PROTEINS;

PLANTS (BOTANY);

CASPASE; CYSTEINE; METACASPASE; NITROUS OXIDE; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; METACASPASE 9, ARABIDOPSIS; NITRIC OXIDE;

ARABIDOPSIS; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME REGULATION; ENZYME REPRESSION; NITROSYLATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FUNCTION; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVATION; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ANIMALIA; ARABIDOPSIS THALIANA; MAMMALIA; METAZOA;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; CASPASES; CYSTEINE; ENZYME ACTIVATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NITRIC OXIDE; PROTEIN STRUCTURE, TERTIARY;

EID: 33847709127     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M608931200     Document Type: Article

References (31)

1. Delledonne, M. (2005) Curr. Opin. Plant Biol. 8, 390-396
2. Stamler, J. S., Jaraki, O., Osborne, J., Simon, D. I., Keaney, J., Vita, J., Singel, D., Valeri, C. R., and Losvalzo, J. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 7674-7677
3. Hess, D. T., Matsumoto, A., Kim, S. O., Marshall, H. E., and Stamler, J. S. (2005) Nat. Rev. Mol. Cell Biol. 6, 150-166
4. Lindermayr, C., Saalbach, G., and Durner, J. (2005) Plant Physiol. 137, 921-930
5. Lindermayr, C., Saalbach, G., Bahnweg, G., and Durner, J. (2006) J. Biol. Chem. 281, 4285-4291
6. Perazzolli, M., Dominici, P., Romero-Puertas, M. C., Zago, E., Zeier, J., Sonoda, M., Lamb, C., and Delledonne, M. (2004) Plant Cell 16, 2785-2794
7. Stamler, J. S., Lamas, S., and Fang, F. C. (2001) Cell 106, 675-683
8. Mannick, J. B., and Schonhoff, C. M. (2004) Free Radic. Res. 38, 1-7
9. Uren, A. G., O'Rourke, K., Aravind, L., Pisabarro, M. T., Seshagiri, S., Koonin, E. V., and Dixit, V. M. (2000) Mol. Cell 6, 961-967
10. Vercammen, D., van de Cotte, B., De Jaeger, G., Eeckhout, D., Casteels, P., Vandepoele, K., Vandenberghe, I., Van Beeumen, J., Inzé, D., and Van Breusegem, F. (2004) J. Biol. Chem. 279, 45329-45336
11. Brüne, B., and Mohr, S. (2001) Curr. Protein Peptide Sci. 2, 61-72
12. Colosimo, A., Xu, Z., Novelli, G., Dallapiccola, B., and Gruenert, D. C. (1999) BioTechniques 26, 870-873
13. Karimi, M., Inzé, D., and Depicker, A. (2002) Trends Plant Sci. 7, 193-195
14. Clough, S. J., and Bent, A. F. (1998) Plant J. 16, 735-743
15. Jaffrey, S. R., Erdjument-Bromage, H., Ferris, C. D., Tempst, P., and Snyder, S. H. (2001) Nat. Cell Biol. 3, 193-197
16. Šali, A., and Blundell, T. L. (1993) J. Mol. Biol. 234, 779-815
17. Chenna, R., Sugawara, H., Koike, T., Lopez, R., Gibson, T. J., Higgins, D. G., and Thompson, J. D. (2003) Nucleic Acids Res. 31, 3497-3500
18. Vercammen, D., Belenghi, B., van de Cotte, B., Beunens, T., Gavigan, J.-A., De Rycke, R., Brackenier, A., Inzé, D., Harris, J. L., and Van Breusegem, F. (2006) J. Mol. Biol. 364, 625-636
19. Mitchell, D. A., and Marletta, M. A. (2005) Nat. Chem. Biol. 1, 154-158
20. Szallies, A., Kubata, B. K., and Duszenko, M. (2002) FEBS Lett. 517, 144-150
21. Mottram, J. C., Helms, M. J., Coombs, G. H., and Sajid, M. (2003) Trends Parasitol. 19, 182-187
22. Woltering, E. J., van der Bent, A., and Hoeberichts, F. A. (2002) Plant Physiol. 130, 1764-1769
23. Madeo, F., Herker, E., Maldener, C., Wissing, S., Lächelt, S., Herlan, M., Fehr, M., Lauber, K., Sigrist, S. J., Wesselborg, S., and Fröhlich, K.-U. (2002) Mol. Cell 9, 911-917
24. Bozhkov, P. V., Suarez, M. F., Filonova, L. H., Daniel, G., Zamyatnin, A. A., Jr., Rodriguez-Nieto, S., Zhivotovsky, B., and Smertenko, A. (2005) Proc. Natl. Acad. Sci. U. S. A. 102, 14463-14468
25. Crawford, M. N. (2006) J. Exp. Bot. 57, 471-478
26. Planchet, E., Gupta, K. J., Sonoda, S., and Kaiser, W. M. (2005) Plant J. 41, 732-743
27. Bethke, P. C., Badger, M. R., and Jones, R. L. (2004) Plant Cell 16, 332-341
28. Correa-Aragunde, N., Graziano, M., and Lamattina, L. (2004) Planta 218, 900-905
29. Gabaldón, C., Gómez Ros, L. V., Pedreño, M. A., and Barceló, A. R. (2005) New Phytol. 165, 121-130
30. Riedl, S. J., Fuentes-Prior, P., Renatus, M., Kairies, N., Krapp, S., Huber, R., Salvesen, G. S., and Bode, W. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 14790-14795
31. DeLano, W. L. (2000) The PyMol Molecular Graphics System, DeLano Scientific, San Carlos, CA